%0 Journal Article
%T Reliable protein folding on non-funneled energy landscapes: the free energy reaction path
%A Gregg Lois
%A Jerzy Blawzdziewicz
%A Corey S. O'Hern
%J Quantitative Biology
%D 2008
%I arXiv
%R 10.1529/biophysj.108.133132
%X A theoretical framework is developed to study the dynamics of protein folding. The key insight is that the search for the native protein conformation is influenced by the rate r at which external parameters, such as temperature, chemical denaturant or pH, are adjusted to induce folding. A theory based on this insight predicts that (1) proteins with non-funneled energy landscapes can fold reliably to their native state, (2) reliable folding can occur as an equilibrium or out-of-equilibrium process, and (3) reliable folding only occurs when the rate r is below a limiting value, which can be calculated from measurements of the free energy. We test these predictions against numerical simulations of model proteins with a single energy scale.
%U http://arxiv.org/abs/0802.0209v1